ID MTF2_MYCS2 Reviewed; 274 AA. AC Q9RMN9; A0QPG8; Q2YHH6; DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 12-AUG-2020, entry version 74. DE RecName: Full=Fatty-acid O-methyltransferase; DE Short=fmt; DE EC=2.1.1.15; GN Name=mtf2; OrderedLocusNames=MSMEI_0386, MSMEG_0393; OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium OS smegmatis). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycolicibacterium. OX NCBI_TaxID=246196; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=ATCC 700084 / mc(2)155; RX PubMed=12368441; DOI=10.1099/00221287-148-10-3079; RA Jeevarajah D., Patterson J.H., McConville M.J., Billman-Jacobe H.; RT "Modification of glycopeptidolipids by an O-methyltransferase of RT Mycobacterium smegmatis."; RL Microbiology 148:3079-3087(2002). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=16194230; DOI=10.1111/j.1365-2958.2005.04847.x; RA Sonden B., Kocincova D., Deshayes C., Euphrasie D., Rhayat L., Laval F., RA Frehel C., Daffe M., Etienne G., Reyrat J.M.; RT "Gap, a mycobacterial specific integral membrane protein, is required for RT glycolipid transport to the cell surface."; RL Mol. Microbiol. 58:426-440(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700084 / mc(2)155; RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., RA Fraser C.M.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700084 / mc(2)155; RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20; RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.; RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic RT mutations or sequencing errors?"; RL Genome Biol. 8:R20.1-R20.9(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700084 / mc(2)155; RX PubMed=18955433; DOI=10.1101/gr.081901.108; RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.; RT "Ortho-proteogenomics: multiple proteomes investigation through orthology RT and a new MS-based protocol."; RL Genome Res. 19:128-135(2009). RN [6] RP IDENTIFICATION. RX PubMed=24826896; DOI=10.1371/journal.pone.0097250; RA Shearer A.G., Altman T., Rhee C.D.; RT "Finding sequences for over 270 orphan enzymes."; RL PLoS ONE 9:E97250-E97250(2014). CC -!- FUNCTION: O-methyltransferase that modifies the hydroxy group of the CC fatty acids. Oleate is the most effective fatty acid acceptor. CC {ECO:0000269|PubMed:12368441}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a fatty acid + S-adenosyl-L-methionine = a fatty acid methyl CC ester + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:23012, CC ChEBI:CHEBI:4986, ChEBI:CHEBI:28868, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789; EC=2.1.1.15; CC -!- DISRUPTION PHENOTYPE: Cells are unable to methylate the CC glycopeptidolipid fatty acids. {ECO:0000269|PubMed:12368441}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=ABK70254.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY138899; AAF05995.1; -; Genomic_DNA. DR EMBL; AY439015; ABB72073.1; -; Genomic_DNA. DR EMBL; CP000480; ABK70254.1; ALT_INIT; Genomic_DNA. DR EMBL; CP001663; AFP36867.1; -; Genomic_DNA. DR RefSeq; WP_014876764.1; NZ_CP009494.1. DR RefSeq; YP_884806.1; NC_008596.1. DR SMR; Q9RMN9; -. DR STRING; 246196.MSMEI_0386; -. DR EnsemblBacteria; ABK70254; ABK70254; MSMEG_0393. DR EnsemblBacteria; AFP36867; AFP36867; MSMEI_0386. DR KEGG; msg:MSMEI_0386; -. DR KEGG; msm:MSMEG_0393; -. DR PATRIC; fig|246196.19.peg.390; -. DR eggNOG; COG2226; Bacteria. DR KO; K22545; -. DR BioCyc; MSME246196:G1H7P-403-MONOMER; -. DR Proteomes; UP000000757; Chromosome. DR Proteomes; UP000006158; Chromosome. DR GO; GO:0030733; F:fatty acid O-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR InterPro; IPR013216; Methyltransf_11. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF08241; Methyltransf_11; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 3: Inferred from homology; KW Methyltransferase; Reference proteome; Transferase. FT CHAIN 1..274 FT /note="Fatty-acid O-methyltransferase" FT /id="PRO_0000430256" SQ SEQUENCE 274 AA; 31353 MW; 41B8DD18ED0F67E1 CRC64; MALGNALVEA RDRVAWRLNI KVAQQAQKLV YRYATRRLKD DDVVFLNYGY EEDPPMGIPL SESDELNRYS IQLYHSTAAQ ADVEGKRVLE VGCGHGGGAS YLARTFRPAT YTGLDLNSDG INFCRRRHNI AGLEFVQGDA QDLPFPDKNF DAVLNVESSH LYPRFDVFLT EVARVLRPGG YFLYTDARPR YDIPEWERAL ADAPLQMLSQ RAINFEVVRG MEKNLDALES VVDRVAPALL RDWIQKYGPA RRAYEELREN TTEYRMYCFV KPAE //